CINS1_SALFT
ID CINS1_SALFT Reviewed; 591 AA.
AC A6XH05;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Cineole synthase 1, chloroplastic {ECO:0000303|PubMed:17557809};
DE Short=Sf-CinS1 {ECO:0000303|PubMed:17557809};
DE EC=4.2.3.108 {ECO:0000269|PubMed:17557809};
DE AltName: Full=Alpha-pinene synthase {ECO:0000303|PubMed:17557809};
DE EC=4.2.3.- {ECO:0000269|PubMed:17557809};
DE AltName: Full=Alpha-terpineol synthase {ECO:0000303|PubMed:17557809};
DE EC=4.2.3.111 {ECO:0000269|PubMed:17557809};
DE AltName: Full=Beta-pinene synthase {ECO:0000303|PubMed:17557809};
DE EC=4.2.3.- {ECO:0000269|PubMed:17557809};
DE AltName: Full=Myrcene synthase {ECO:0000303|PubMed:17557809};
DE EC=4.2.3.15 {ECO:0000269|PubMed:17557809};
DE AltName: Full=Sabinene synthase {ECO:0000303|PubMed:17557809};
DE EC=4.2.3.- {ECO:0000269|PubMed:17557809};
DE Flags: Precursor;
GN Name=CinS1 {ECO:0000303|PubMed:17557809};
OS Salvia fruticosa (Greek sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=268906;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-591, NUCLEOTIDE SEQUENCE
RP [MRNA], FUNCTION, MUTAGENESIS OF ASN-338; ALA-339; GLY-447; ILE-449 AND
RP PRO-450, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SITE.
RX PubMed=17557809; DOI=10.1105/tpc.106.047779;
RA Kampranis S.C., Ioannidis D., Purvis A., Mahrez W., Ninga E.,
RA Katerelos N.A., Anssour S., Dunwell J.M., Degenhardt J., Makris A.M.,
RA Goodenough P.W., Johnson C.B.;
RT "Rational conversion of substrate and product specificity in a Salvia
RT monoterpene synthase: structural insights into the evolution of terpene
RT synthase function.";
RL Plant Cell 19:1994-2005(2007).
CC -!- FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of
CC monoterpene natural products, components of the chemical defense
CC arsenal (PubMed:17557809). Catalyzes the conversion of (2E)-geranyl
CC diphosphate (GPP) into 1,8-cineole, and, as minor products, alpha-
CC terpineol, beta-pinene, alpha-pinene, sabinene and myrcene
CC (PubMed:17557809). {ECO:0000269|PubMed:17557809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate;
CC Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108;
CC Evidence={ECO:0000269|PubMed:17557809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32544;
CC Evidence={ECO:0000269|PubMed:17557809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17557809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663;
CC Evidence={ECO:0000269|PubMed:17557809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-pinene + diphosphate;
CC Xref=Rhea:RHEA:25666, ChEBI:CHEBI:33019, ChEBI:CHEBI:50025,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17557809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25667;
CC Evidence={ECO:0000269|PubMed:17557809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol +
CC diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC EC=4.2.3.111; Evidence={ECO:0000269|PubMed:17557809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552;
CC Evidence={ECO:0000269|PubMed:17557809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:17557809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC Evidence={ECO:0000269|PubMed:17557809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene;
CC Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17557809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637;
CC Evidence={ECO:0000269|PubMed:17557809};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=65.4 uM for (2E)-geranyl diphosphate
CC {ECO:0000269|PubMed:17557809};
CC Note=kcat is 3.18 min(-1) with (2E)-geranyl diphosphate as substrate.
CC {ECO:0000269|PubMed:17557809};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:17557809}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ785793; ABH07677.1; -; mRNA.
DR PDB; 2J5C; X-ray; 1.95 A; A/B=25-591.
DR PDBsum; 2J5C; -.
DR SMR; A6XH05; -.
DR BRENDA; 4.2.3.108; 12982.
DR UniPathway; UPA00213; -.
DR EvolutionaryTrace; A6XH05; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102313; F:1,8-cineole synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IDA:UniProtKB.
DR GO; GO:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR GO; GO:0080015; F:sabinene synthase activity; IDA:UniProtKB.
DR GO; GO:0046248; P:alpha-pinene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016099; P:monoterpenoid biosynthetic process; IDA:UniProtKB.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Lyase; Magnesium; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..591
FT /note="Cineole synthase 1, chloroplastic"
FT /id="PRO_0000455078"
FT MOTIF 345..349
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A6XH06"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT SITE 338
FT /note="Confers catalytic properties (activation of water
FT molecule and hydroxylation of the alpha-terpinyl cation)"
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 338
FT /note="N->A,C: Acquired ability to produce cis-alpha-
FT bergamotene, trans-alpha-bergamotene, Z-beta-farnesene, E-
FT beta-farnesene, beta-selinene, beta-bisabolene and beta-
FT sesquiphellandrene from farnesyl diphosphate (FPP), thus
FT having a sesquiterpene synthase activity."
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 338
FT /note="N->I: Lost ability to produce 1,8-cineole, beta-
FT pinene and alpha-terpineol, but increased ability to
FT produce sabinene and acquired ability to produce limonene
FT from (2E)-geranyl diphosphate. Lost ability to produce 1,8-
FT cineole, beta-pinene and alpha-terpineol, but strongly
FT increased ability to produce sabinene and acquired ability
FT to produce limonene from (2E)-geranyl diphosphate; when
FT associated with T-339. Lost ability to produce 1,8-cineole,
FT alpha-pinene, beta-pinene and alpha-terpineol, but strongly
FT increased ability to produce sabinene and slightly acquired
FT ability to produce limonene from (2E)-geranyl diphosphate;
FT when associated with T-339, S-447, P-449 and T-450."
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 338
FT /note="N->S: Acquired ability to produce E-beta-farnesene,
FT beta-bisabolene and beta-sesquiphellandrene from farnesyl
FT diphosphate (FPP), thus having a sesquiterpene synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 339
FT /note="A->T: Lost ability to produce 1,8-cineole, but
FT strongly increased ability to produce sabinene and acquired
FT ability to produce limonene from (2E)-geranyl diphosphate;
FT when associated with I-338. Lost ability to produce 1,8-
FT cineole, alpha-pinene, beta-pinene and alpha-terpineol, but
FT strongly increased ability to produce sabinene and slightly
FT acquired ability to produce limonene from (2E)-geranyl
FT diphosphate; when associated with I-338, S-447, P-449 and
FT T-450."
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 447
FT /note="G->S: Lost ability to produce 1,8-cineole, alpha-
FT pinene, beta-pinene and alpha-terpineol, but strongly
FT increased ability to produce sabinene and slightly acquired
FT ability to produce limonene from (2E)-geranyl diphosphate;
FT when associated with I-338, T-339, P-449 and T-450."
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 449
FT /note="I->P: Impaired terpene synthase activity; when
FT associated with S-447. Lost ability to produce 1,8-cineole,
FT alpha-pinene, beta-pinene and alpha-terpineol, but strongly
FT increased ability to produce sabinene and slightly acquired
FT ability to produce limonene from (2E)-geranyl diphosphate;
FT when associated with I-338, T-339, S-447 and T-450."
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 450
FT /note="P->T: Lost ability to produce 1,8-cineole, alpha-
FT pinene, beta-pinene and alpha-terpineol, but strongly
FT increased ability to produce sabinene and slightly acquired
FT ability to produce limonene from (2E)-geranyl diphosphate;
FT when associated with I-338, T-339, S-447 and P-449."
FT /evidence="ECO:0000269|PubMed:17557809"
FT HELIX 85..101
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:2J5C"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 267..298
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 328..349
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 354..366
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 377..401
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 406..429
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 435..445
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 449..458
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 465..471
FT /evidence="ECO:0007829|PDB:2J5C"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 476..492
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 519..542
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 547..563
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:2J5C"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:2J5C"
SQ SEQUENCE 591 AA; 69613 MW; C59A0560F9F80853 CRC64;
MSSLIMQVVI PKPAKFFHNN LFSLSSKRHR FSTTTTTRGG RWARCSLQTG NEIQTERRTG
GYQPTLWDFS TIQSFDSEYK EEKHLMRAAG MIDQVKMMLQ EEVDSIRRLE LIDDLRRLGI
SCHFEREIVE ILNSKYYTNN EIDERDLYST ALRFRLLRQY DFSVSQEVFD CFKNAKGTDF
KPSLVDDTRG LLQLYEASFL SAQGEETLRL ARDFATKFLQ KRVLVDKDIN LLSSIERALE
LPTHWRVQMP NARSFIDAYK RRPDMNPTVL ELAKLDFNMV QAQFQQELKE ASRWWNSTGL
VHELPFVRDR IVECYYWTTG VVERRQHGYE RIMLTKINAL VTTIDDVFDI YGTLEELQLF
TTAIQRWDIE SMKQLPPYMQ ICYLALFNFV NEMAYDTLRD KGFDSTPYLR KVWVGLIESY
LIEAKWYYKG HKPSLEEYMK NSWISIGGIP ILSHLFFRLT DSIEEEAAES MHKYHDIVRA
SCTILRLADD MGTSLDEVER GDVPKSVQCY MNEKNASEEE AREHVRSLID QTWKMMNKEM
MTSSFSKYFV EVSANLARMA QWIYQHESDG FGMQHSLVNK MLRDLLFHRY E
